Expressional patterns of chaperones in ten human tumor cell lines

Jae-Kyung Myung,Gert Lubec,Leila Afjehi-Sadat,Irene Slavc,Maureen Felizardo-Cabatic

doi:10.1186/1477-5956-2-8

Abstract

BackgroundChaperones (CH) play an important role in tumor biology but no systematic work on expressional patterns has been reported so far. The aim of the study was therefore to present an analytical method for the concomitant determination of several CH in human tumor cell lines, to generate expressional patterns in the individual cell lines and to search for tumor and non-tumor cell line specific CH expression.Human tumor cell lines of neuroblastoma, colorectal and adenocarcinoma of the ovary, osteosarcoma, rhabdomyosarcoma, malignant melanoma, lung, cervical and breast cancer, promyelocytic leukaemia were homogenised, proteins were separated on two-dimensional gel electrophoresis with in-gel digestion of proteins and MALDI-TOF/TOF analysis was carried out for the identification of CH.ResultsA series of CH was identified including the main CH groups as HSP90/HATPas_C, HSP70, Cpn60_TCP1, DnaJ, Thioredoxin, TPR, Pro_isomerase, HSP20, ERP29_C, KE2, Prefoldin, DUF704, BAG, GrpE and DcpS.ConclusionsThe ten individual tumor cell lines showed different expression patterns, which are important for the design of CH studies in tumor cell lines. The results can serve as a reference map and form the basis of a concomitant determination of CH by a protein chemical rather than an immunochemical method, independent of antibody availability or specificity.

Highlights

Chaperones (CH) play an important role in tumor biology but no systematic work on expressional patterns has been reported so far
This study addresses the question of differential chaperone expression studied in ten different tumor and three normal cell lines using 2-DE and matrix-assisted laser desorption/ionization-mass spectrometry (MALDI-TOF/ TOF) allowing concomitant determination of many CH at the protein chemical level rather than by immunochemical methods, independent of antibody availability and specificity
The contribution of heat shock proteins (HSPs) to tumorigenesis may be attributed to their pleiotropic activities as molecular chaperones that provide the cancer cell with an opportunity to alter protein activities, in particular components of the cell cycle machinery, kinases and other proteins implicated in tumor progression

Summary

Introduction

Chaperones (CH) play an important role in tumor biology but no systematic work on expressional patterns has been reported so far. Efforts from a large number of investigators have shown that the heat shock response is ubiquitous and highly conserved. CH form an essential defense mechanism for protection of cells from a variety of harmful conditions, including temperature elevation or heat shock, decrease in pH, hypersalinity, alcohols, heavy metals, oxidative stress, inhibitors of energy metabolism, fever or inflammation [2,3]. This broad spectrum of functions gave rise to the term 'molecular chaperone' an entity that acts to assist other proteins' folding and maturation (page number not for citation purposes)

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